Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 20, Pages 6377-6382Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1418736112
Keywords
dynamin-like protein; organelle fission; GTPase activating protein; DLP; GAP
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Funding
- Netherlands Organisation for Scientific Research (NWO) [821.02.022, 723.013.004]
- European Union Marie Curie Intra-European Fellowship [FP7-330150]
- research program of the Kluyver Centre for Genomics of Industrial Fermentation, Netherlands Genomics Initiative/NWO
- Biotechnology and Biological Sciences Research Council [BB/K006231/1]
- Wellcome Trust Institutional Strategic Support Award [WT097835MF]
- Marie Curie Initial Training Networks Action PerFuMe [316723]
- BBSRC [BB/K006231/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K006231/1] Funding Source: researchfish
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The initial phase of peroxisomal fission requires the peroxisomal membrane protein Peroxin 11 (Pex11p), which remodels the membrane, resulting in organelle elongation. Here, we identify an additional function for Pex11p, demonstrating that Pex11p also plays a crucial role in the final step of peroxisomal fission: dynamin-like protein (DLP)-mediated membrane scission. First, we demonstrate that yeast Pex11p is necessary for the function of the GTPase Dynamin-related 1 (Dnm1p) in vivo. In addition, our data indicate that Pex11p physically interacts with Dnm1p and that inhibiting this interaction compromises peroxisomal fission. Finally, we demonstrate that Pex11p functions as a GTPase activating protein (GAP) for Dnm1p in vitro. Similar observations were made for mammalian Pex11 beta and the corresponding DLP Drp1, indicating that DLP activation by Pex11p is conserved. Our work identifies a previously unknown requirement for a GAP in DLP function.
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